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Originally published In Press as doi:10.1074/jbc.M006697200 on December 11, 2000

J. Biol. Chem., Vol. 276, Issue 10, 7661-7671, March 9, 2001
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Transcriptional Activation of the Rat Vesicular Monoamine Transporter 2 Promoter in Gastric Epithelial Cells
REGULATION BY GASTRIN*

Fiona WatsonDagger , Rachel S. Kiernan, Damian G. Deavall, Andrea Varro, and Rod Dimaline

From the Physiological Laboratory, University of Liverpool, Liverpool L69 3BX, United Kingdom

Vesicular monoamine transporter 2 is important for the accumulation of monoamine neurotransmitters into synaptic vesicles and histamine transport into secretory vesicles of the enterochromaffin-like cell of the gastric corpus. In this study we have investigated the mechanisms regulating the transcriptional activation of the rat vesicular monoamine transporter 2 (VMAT2) promoter in gastric epithelial cells. Maintenance of basal levels of transcription was dependent on the presence of SP1, cAMP-response element (CRE), and overlapping AP2/SP1 consensus sequences within the region of promoter from -86 to +1 base pairs (bp). Gastrin stimulation increased transcriptional activity, and responsiveness was shown to be dependent on the CRE (-33 to -26 bp) and AP2/SP1 (-61 to -48 bp) consensus sites but independent of the SP1 site at -86 to -81 bp. Gastrin-induced transcription was dependent on the cooperative interaction of an uncharacterized nuclear factor of ~23.3 kDa that bound to the putative AP2/SP1 site, CRE-binding protein (CREB), and CREB-binding protein/p300. Gastrin stimulation resulted in the increased binding of phosphorylated CREB to the promoter, but it did not result in the increased binding of the AP2/SP1-binding protein. The gastrin responsiveness of the promoter was shown to be dependent on both the protein kinase C and mitogen-activated protein kinase/extracellular signal-regulated kinase kinase-signaling pathways, which may converge on the AP2/SP1-binding protein.


* This work was supported by Wellcome Trust Grant 050830.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: The Physiological Laboratory, University of Liverpool, Crown St., Liverpool L69 3BX, UK. E-mail: watso@liv.ac.uk.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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